Abstract
At present there is a surge in interest in biophysical research aimed at elucidating collective interactions between cellular proteins and associated biomolecules leading to supramolecular structures, with the ultimate goal of relating structure to function. The nerve cell cytoskeleton provides a rich example of highly ordered bundles and networks of interacting neurofilaments, microtubules and filamentous actin, where the nature of the interactions, structures and structure-function correlations remain poorly understood. We present synchrotron X-ray diffraction and electron microscopy data, in reconstituted protein systems from the bovine central nervous system, which reveal unexpected structures not predicted by current electrostatic theories. By mixing preassembled microtubules with charged membranes or polypeptides we found hierarchical bionanotubes made of microtubules coated by lipid bilayers or polypeptides, which in turn are coated with a third layer of tubulin oligomers forming rings or spirals.
Original language | English |
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Pages (from-to) | s83-s87 |
Journal | Journal of Applied Crystallography |
Volume | 40 |
Issue number | SUPPL. 1 |
DOIs | |
State | Published - Apr 2007 |
Keywords
- Lipids
- Microtubule
- Multivalent cations
- Polypeptides
- Tubulin
- X-ray scattering